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Literature summary for 1.14.11.47 extracted from

  • Van Staalduinen, L.; Novakowski, S.; Jia, Z.
    Structure and functional analysis of YcfD, a novel 2-oxoglutarate/Fe2+-dependent oxygenase involved in translational regulation in Escherichia coli (2014), J. Mol. Biol., 426, 1898-1910.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant E146A/K147A, predicted to enhance crystallizability, to 2.7 A resolution, space group P43212 with a single protein molecule in the asymmetric unit. The N-terminal domain contains the signature DSBH or beta-barrel that is characteristic of 2OG-dependent oxygenases. The core DSBH is made up of two beta-sheets, one composed of five strands and the second one composed of three strands Escherichia coli

Protein Variants

Protein Variants Comment Organism
E146A/K147A mutation predicted to enhance crystallizability Escherichia coli
R140A loss of binding of 2-oxoglutarate Escherichia coli
S116A loss of binding of 2-oxoglutarate Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P27431
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information binding of 2-oxoglutarate to isoform YcfD occurs in an exothermic manner, dissociation constant is 55.6 microM. Residues S116 and R140 are involved in binding Escherichia coli ?
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Synonyms

Synonyms Comment Organism
50S ribosomal protein L16 arginine hydroxylase
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Escherichia coli
ycfD
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Escherichia coli

General Information

General Information Comment Organism
physiological function overexpression of L16 arginine hydroxylase YcfD inhibits cell growth signifying a toxic effect on ribosome assembly. The enzyme interacts with ribosomal protein RL-16 of the 50S subunit Escherichia coli